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Spatiotemporally direct capturing global substrates of post-translational modifying enzymes in living cells

ABSTRACT: Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of protein-modifying enzymes via PTM-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner.

ORGANISM(S): Escherichia Coli

SUBMITTER: Minjia Tan

PROVIDER: PXD040318 | iProX | Wed Feb 22 00:00:00 GMT 2023

REPOSITORIES: iProX

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Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.

Hu Hao H Hu Wei W Guo An-Di AD Zhai Linhui L Ma Song S Nie Hui-Jun HJ Zhou Bin-Shan BS Liu Tianxian T Jia Xinglong X Liu Xing X Yao Xuebiao X Tan Minjia M Chen Xiao-Hua XH

Nature communications 20240217 1

Protein-modifying enzymes regulate the dynamics of myriad post-translational modification (PTM) substrates. Precise characterization of enzyme-substrate associations is essential for the molecular basis of cellular function and phenotype. Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of lysine-modifying enzymes via PTM-acceptor residue cros ...[more]

PMID: 38368419

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